F
IPR000763

Catalase-peroxidase haem

InterPro entry
Short nameCatalase_peroxidase
Overlapping
homologous
superfamilies
 

Description

Haem-containing catalase-peroxidases are bifunctional antioxidant enzymes that exhibit both catalase (
1.11.1.6
) and peroxidase (
1.11.1.7
) activity, and which are present predominantly in bacterial species
[6]
. Several evolutionary lineages are present also in archaeal, fungal, and protistan species. These enzymes provide protection against oxidative stress by dismutating hydrogen peroxide to oxygen and water
[7]
. Phylogenetically they are closely related to ascorbate peroxidases and cytochrome c peroxidases
[5]
and can be divided in two distinct clades
[2]
. They do not share sequence similarity with mono-functional, haem-containing catalases (
IPR002226
) that are ubiquitous in aerobic organisms, nor with non-haem manganese-containing catalases found in bacteria (
IPR007760
). Catalases perform a unique two-step reaction cycle that cleaves two hydrogen peroxide molecules heterolytically to alternately oxidise and reduce the haem iron thus releasing water and molecular oxygen
[7]
. Contrary, peroxidases use hydrogen peroxide only to oxidise the haem iron, but use different electron donors such as NADH or ascorbate to then reduce the haem.

The structure of the catalase-peroxidase from the archaeon, Haloarcula marismortui (Halobacterium marismortui), reveals a dimer of two identical subunits
[1]
, although some catalase-peroxidases can exist also as homotetramers. The general topology, as well as the arrangement of the catalytic residues and haem in the active site, are similar to other class I peroxidases. However, the location of the haem group deeply buried inside the domain is typical of a catalase. The primary structure of the subunit can be divided into two similar halves, which very probably arose from a gene duplication event
[5, 3]
. A similar structure was obtained also for a catalase-peroxidase from the proteobacterium Burkholderia pseudomallei
[4]
.

References

1.The 2.0 A crystal structure of catalase-peroxidase from Haloarcula marismortui. Yamada Y, Fujiwara T, Sato T, Igarashi N, Tanaka N. Nat. Struct. Biol. 9, 691-5, (2002). View articlePMID: 12172540

2.Molecular diversity of katG genes in the soil bacteria Comamonas. Godocikova J, Zamocky M, Buckova M, Obinger C, Polek B. Arch. Microbiol. (2010). PMID: 20062977

3.Phylogenetic relationships in class I of the superfamily of bacterial, fungal, and plant peroxidases. Zamocky M. Eur. J. Biochem. 271, 3297-309, (2004). View articlePMID: 15291807

4.Catalase-peroxidase KatG of Burkholderia pseudomallei at 1.7A resolution. Carpena X, Loprasert S, Mongkolsuk S, Switala J, Loewen PC, Fita I. J. Mol. Biol. 327, 475-89, (2003). View articlePMID: 12628252

5.Bacterial catalase-peroxidases are gene duplicated members of the plant peroxidase superfamily. Welinder KG. Biochim. Biophys. Acta 1080, 215-20, (1991). PMID: 1954228

6.Occurrence, phylogeny, structure, and function of catalases and peroxidases in cyanobacteria. Bernroitner M, Zamocky M, Furtmuller PG, Peschek GA, Obinger C. J. Exp. Bot. 60, 423-40, (2009). View articlePMID: 19129167

7.Evolution of catalases from bacteria to humans. Zamocky M, Furtmuller PG, Obinger C. Antioxid. Redox Signal. 10, 1527-48, (2008). View articlePMID: 18498226

GO terms

Cross References

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